View source for 9rnz


==Atomic resolution (1.02 A) XFEL structure of nitrite-bound copper nitrite reductase from Bradyrhizobium sp. determined by serial femtosecond rotation crystallography (SF-ROX) at 100 K==
<StructureSection load='9rnz' size='340' side='right'caption='[[9rnz]], [[Resolution|resolution]] 1.02&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9rnz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bradyrhizobium_diazoefficiens_USDA_110 Bradyrhizobium diazoefficiens USDA 110]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9RNZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9RNZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.02&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NO2:NITRITE+ION'>NO2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9rnz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9rnz OCA], [https://pdbe.org/9rnz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9rnz RCSB], [https://www.ebi.ac.uk/pdbsum/9rnz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9rnz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q89EJ6_BRADU Q89EJ6_BRADU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Metalloproteins represent a major fraction of the protein kingdom and often exploit the redox chemistry of transition metals to drive key biological events involving proton and electron transfer. Copper is one of the most widely used transition metals whose redox properties are utilised in both electron transfer and catalysis of chemical substrates. Copper nitrite reductases (CuNiRs) utilise two types of copper centres and have become a model system for studying complex biological events that underpin the reaction mechanisms of redox enzymes, including proton-coupled electron transfer and substrate gating. We utilised the higher X-ray energy (13 keV) available at the SACLA X-ray Free Electron Laser (XFEL) and SHELXL refinement to obtain accurate atomic resolution structures of CuNiRs at ~1 A from three organisms - in the oxidised (low and high pH), reduced and substrate-bound states. A consistent picture now emerges with the observation of a pentacoordinated oxidised catalytic type-2 Cu (T2Cu(2+)) centre in all cases. A tetracoordinated reduced T2Cu(+) site with a single solvent ligand has also been captured, giving structural support to the random-sequential scheme with ordered pathway being dominant.

Accurate atomic resolution XFEL structures of a metalloenzyme reveal key insights into its catalytic mechanism.,Rose SL, Antonyuk S, Ferroni FF, Sugimoto H, Yamashita K, Hirata K, Ago H, Ueno G, Murakami H, Eady RR, Tosha T, Yamamoto M, Hasnain SS Nat Commun. 2026 Mar 7. doi: 10.1038/s41467-026-70261-1. PMID:41794770<ref>PMID:41794770</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9rnz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bradyrhizobium diazoefficiens USDA 110]]
[[Category: Large Structures]]
[[Category: Ago H]]
[[Category: Antonyuk SV]]
[[Category: Eady RR]]
[[Category: Ferroni FM]]
[[Category: Hasnain SS]]
[[Category: Hirata K]]
[[Category: Murakami H]]
[[Category: Rose SL]]
[[Category: Sugimoto H]]
[[Category: Tosha T]]
[[Category: Ueno G]]
[[Category: Yamamoto M]]
[[Category: Yamashita K]]